Document Detail


Adsorption and disruption of lipid bilayers by nanoscale protein aggregates.
MedLine Citation:
PMID:  22276744     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Nanoparticles taken into biological systems can have biological impacts through their interactions with cell membranes, accompanied by protein adsorption onto the nanoparticle surfaces, forming a so-called protein corona. Our current research aims to demonstrate that nanoscale protein aggregates behave like such nanoparticles with regard to the interaction with lipid membranes. In this study, the adsorption and disruption of the lipid membranes by protein aggregates were investigated using amyloid fibrils and nanoscale thermal aggregates of lysozyme. Both types of protein aggregate had disruptive effects on the negatively charged liposomes, similar to polycationic nanoparticles. Interestingly, adsorption of liposomes on the amyloid fibrils preceding disruption occurred even if the net charge of the liposome was zero, suggesting the importance of hydrophobic interactions in addition to electrostatic interactions. The results of the present study provide new insights into the biological impacts of nanoparticles in vivo.
Authors:
Atsushi Hirano; Hiroki Yoshikawa; Shuhei Matsushita; Yoichi Yamada; Kentaro Shiraki
Related Documents :
2493134 - Kin, a mammalian nuclear protein immunologically related to e. coli reca protein.
3136804 - Isolation and characterization of an 18 kda hypusine-containing protein from cultured n...
20491474 - Maize 27 kda gamma-zein is a potential allergen for early weaned pigs.
1714514 - Proteolytic processing of pol-tyb proteins from the yeast retrotransposon ty1.
18327764 - Semaphorin 3a inhibits erm protein phosphorylation in growth cone filopodia through ina...
18234734 - The value of serial cerebrospinal fluid 14-3-3 protein levels in adult community-acquir...
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-1-25
Journal Detail:
Title:  Langmuir : the ACS journal of surfaces and colloids     Volume:  -     ISSN:  1520-5827     ISO Abbreviation:  -     Publication Date:  2012 Jan 
Date Detail:
Created Date:  2012-1-26     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9882736     Medline TA:  Langmuir     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Anti-miR-155 oligonucleotide enhances chemosensitivity of U251 cell to taxol by inducing apoptosis.
Next Document:  Predictive value of HIV-1 replication capacity and phenotypic susceptibility scores in antiretrovira...